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Infection and Immunity, October 2003, p. 5514-5522, Vol. 71, No. 10
0019-9567/03/$08.00+0     DOI: 10.1128/IAI.71.10.5514-5522.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Kinome Analysis of Host Response to Mycobacterial Infection: a Novel Technique in Proteomics

Department of Medicine, Division of Infectious Diseases, University of British Columbia. Vancouver, British Columbia V5Z 3J5, Canada

Received 15 April 2003/ Returned for modification 4 June 2003/ Accepted 3 July 2003

An array of mammalian phospho-specific antibodies was used to screen for a host response upon mycobacterial infection, reflected as changes in host protein phosphorylation. Changes in the phosphorylation state of 31 known signaling molecules were tracked after infection with live or heat killed Mycobacterium bovis BCG or after incubation with the mycobacterial cell wall component lipoarabinomannan (LAM). Mycobacterial infection triggers a signaling cascade leading to activation of stress-activated protein kinase and its subsequent downstream target, c-Jun. Mycobacteria were also shown to inhibit the activation of protein kinase C and to induce phosphorylation of proteins not yet known to be involved in mycobacterial infection, such as the cytoskeletal protein -adducin, glycogen synthase kinase 3ß, and a receptor subunit involved in regulation of intracellular Ca²⁺ levels. The mycobacterial cell wall component LAM has been identified as a trigger for some of these modulation events.

Editor: W. A. Petri, Jr.

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